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Protein

Retinoid-binding protein 7

Gene

RBP7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Intracellular transport of retinol.1 Publication

GO - Molecular functioni

Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Retinol-binding, Vitamin A

Names & Taxonomyi

Protein namesi
Recommended name:
Retinoid-binding protein 7
Alternative name(s):
Cellular retinoic acid-binding protein 4
Short name:
CRABP4
Short name:
CRBP4
Cellular retinoic acid-binding protein IV
Short name:
CRABP-IV
Gene namesi
Name:RBP7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:30316. RBP7.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134988307.

Chemistry

DrugBankiDB00162. Vitamin A.

Polymorphism and mutation databases

BioMutaiRBP7.
DMDMi20139582.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 134134Retinoid-binding protein 7PRO_0000067403Add
BLAST

Proteomic databases

MaxQBiQ96R05.
PaxDbiQ96R05.
PRIDEiQ96R05.

Expressioni

Tissue specificityi

Expressed primarily in kidney, heart and transverse colon. Detected in adult lymph node, appendix, ascending colon, and in fetal heart and spleen.1 Publication

Gene expression databases

BgeeiQ96R05.
CleanExiHS_RBP7.
ExpressionAtlasiQ96R05. baseline and differential.
GenevisibleiQ96R05. HS.

Organism-specific databases

HPAiHPA034749.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
PIK3R3Q925693EBI-2856326,EBI-79893
SOCS4Q8WXH53EBI-2856326,EBI-3942425

Protein-protein interaction databases

BioGridi125500. 6 interactions.
IntActiQ96R05. 7 interactions.
STRINGi9606.ENSP00000294435.

Structurei

Secondary structure

1
134
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 1610Combined sources
Helixi17 – 248Combined sources
Helixi28 – 347Combined sources
Beta strandi40 – 467Combined sources
Beta strandi49 – 557Combined sources
Beta strandi61 – 666Combined sources
Beta strandi71 – 744Combined sources
Turni76 – 794Combined sources
Beta strandi82 – 909Combined sources
Beta strandi93 – 11220Combined sources
Beta strandi115 – 1228Combined sources
Beta strandi125 – 1339Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LPJX-ray2.00A2-134[»]
ProteinModelPortaliQ96R05.
SMRiQ96R05. Positions 2-134.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96R05.

Family & Domainsi

Domaini

Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG4015. Eukaryota.
ENOG4111US8. LUCA.
GeneTreeiENSGT00760000118898.
HOGENOMiHOG000004831.
HOVERGENiHBG005633.
InParanoidiQ96R05.
OMAiRNYLVKF.
PhylomeDBiQ96R05.
TreeFamiTF316894.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
IPR031259. iLBP.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
IPR033075. RBP7.
[Graphical view]
PANTHERiPTHR11955. PTHR11955. 1 hit.
PTHR11955:SF77. PTHR11955:SF77. 1 hit.
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00214. FABP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q96R05-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPADLSGTWT LLSSDNFEGY MLALGIDFAT RKIAKLLKPQ KVIEQNGDSF
60 70 80 90 100
TIHTNSSLRN YFVKFKVGEE FDEDNRGLDN RKCKSLVIWD NDRLTCIQKG
110 120 130
EKKNRGWTHW IEGDKLHLEM FCEGQVCKQT FQRA
Length:134
Mass (Da):15,536
Last modified:December 1, 2001 - v1
Checksum:iB152C8B3D95B20BD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY145438 mRNA. Translation: AAN61071.1.
AF399927 mRNA. Translation: AAK85409.1.
AK312027 mRNA. Translation: BAG34964.1.
AL603962, AL590639 Genomic DNA. Translation: CAI16811.1.
AL590639, AL603962 Genomic DNA. Translation: CAI14685.1.
CH471130 Genomic DNA. Translation: EAW71638.1.
BC063013 mRNA. Translation: AAH63013.1.
CCDSiCCDS109.1.
RefSeqiNP_443192.1. NM_052960.2.
UniGeneiHs.422688.

Genome annotation databases

EnsembliENST00000294435; ENSP00000294435; ENSG00000162444.
GeneIDi116362.
KEGGihsa:116362.
UCSCiuc001aqq.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY145438 mRNA. Translation: AAN61071.1.
AF399927 mRNA. Translation: AAK85409.1.
AK312027 mRNA. Translation: BAG34964.1.
AL603962, AL590639 Genomic DNA. Translation: CAI16811.1.
AL590639, AL603962 Genomic DNA. Translation: CAI14685.1.
CH471130 Genomic DNA. Translation: EAW71638.1.
BC063013 mRNA. Translation: AAH63013.1.
CCDSiCCDS109.1.
RefSeqiNP_443192.1. NM_052960.2.
UniGeneiHs.422688.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LPJX-ray2.00A2-134[»]
ProteinModelPortaliQ96R05.
SMRiQ96R05. Positions 2-134.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125500. 6 interactions.
IntActiQ96R05. 7 interactions.
STRINGi9606.ENSP00000294435.

Chemistry

DrugBankiDB00162. Vitamin A.

Polymorphism and mutation databases

BioMutaiRBP7.
DMDMi20139582.

Proteomic databases

MaxQBiQ96R05.
PaxDbiQ96R05.
PRIDEiQ96R05.

Protocols and materials databases

DNASUi116362.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000294435; ENSP00000294435; ENSG00000162444.
GeneIDi116362.
KEGGihsa:116362.
UCSCiuc001aqq.4. human.

Organism-specific databases

CTDi116362.
GeneCardsiRBP7.
HGNCiHGNC:30316. RBP7.
HPAiHPA034749.
MIMi608604. gene.
neXtProtiNX_Q96R05.
PharmGKBiPA134988307.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4015. Eukaryota.
ENOG4111US8. LUCA.
GeneTreeiENSGT00760000118898.
HOGENOMiHOG000004831.
HOVERGENiHBG005633.
InParanoidiQ96R05.
OMAiRNYLVKF.
PhylomeDBiQ96R05.
TreeFamiTF316894.

Miscellaneous databases

ChiTaRSiRBP7. human.
EvolutionaryTraceiQ96R05.
GenomeRNAii116362.
PROiQ96R05.
SOURCEiSearch...

Gene expression databases

BgeeiQ96R05.
CleanExiHS_RBP7.
ExpressionAtlasiQ96R05. baseline and differential.
GenevisibleiQ96R05. HS.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
IPR031259. iLBP.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
IPR033075. RBP7.
[Graphical view]
PANTHERiPTHR11955. PTHR11955. 1 hit.
PTHR11955:SF77. PTHR11955:SF77. 1 hit.
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00214. FABP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Ligand binding and structural analysis of a human putative cellular retinol-binding protein."
    Folli C., Calderone V., Ramazzina I., Zanotti G., Berni R.
    J. Biol. Chem. 277:41970-41977(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), FUNCTION, CHARACTERIZATION, TISSUE SPECIFICITY.
  2. Guo J.H., She X.Y., Dai F.Y., Yu L.
    Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Substantia nigra.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Pancreas.

Entry informationi

Entry nameiRET7_HUMAN
AccessioniPrimary (citable) accession number: Q96R05
Secondary accession number(s): B2R517, Q5SWJ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2002
Last sequence update: December 1, 2001
Last modified: June 8, 2016
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.